New looks at old proteins

Cells rely on organs to protect themselves from the outside world. But these organs cannot be completely shut down because nutrients and other molecules have to go through them. To achieve this, a cell membrane has many types of channels and pores. Also, there are receptors, antennas if you will, that are activated in the membrane that continuously monitor the outside world and signal to the inside of the cell. Extensive collaboration between five VIB groups has led to a better understanding of the tools that plants use to regulate the protein composition of the external organs. This find, published in Advances in science, advancing our basic knowledge of how plasma membrane composition can be altered based on external stimuli, an essential process for life on earth.

TPLATE molecular architecture

Complex life, also called eukaryotic cells, has complex cells. Unlike bacteria, for example, there are many specific internal regions in complex life cells called organelles. These organelles exchange substances among themselves. To do that, the organelles have a few tricks. One of those tricks is vesicle exchange. This means that they use part of their own membrane as a bag for the goods to be exchanged.

Recent discoveries have shown that plants rely heavily on a protein complex called TPLATE to do so. This complex is found not only in plants, but also in a wide range of other eukaryotes, which appear to be a very old microbial and part of a complex protein family from which all other members scrutinized closely. However, since this particular complex is not present in the most studied organism models (animals and yeast), its existence and function remained under the radar for a long time.

In this study, VIB teams (the groups of Bert De Rybel, Geert De Jaeger, and Daniël Van Damme from the VIB-UGent Center for Plant Systems Biology, Remy Loris from the VIB-VIB Center for Structural Biology, and Savvas Savvides from The VIB-UGent Center for Inflammation Research) will feature TPLATE molecular architecture for the first time. They achieved this by crossing mass spectrametry and computer simulations. These new insights revealed the direction of this complex toward the membrane as well as the delicate relationship between the different areas of the substrate.

These findings are important to increase our knowledge of vital eukaryotic processes. In fact, the structure of this complex now allows us to compare it with the known structures of close relatives present in all eukaryotes including animals and yeast and this allows us to average -see the growth of these trade centers.

Working together for success

Achieving both a structured and a functional view of this enigmatic complex required a unified and collaborative approach. Five VIB research groups and one Czech Republic group added their expertise to conduct experiments ranging from lipid binding studies to structural biology techniques.

The novel structural view was created mainly based on crosslinking mass spectrametry, played with the help of the main VIB Proteomics tool.

A key benefit of working at VIB is that it greatly encourages and enables access to knowledge and experience that allows research organizations to embark on joint projects that go far beyond their comfort zone. ‘- Professor Daniel Van Damme

This study will form the basis of further scientific work and will open doors for the generation of novel and safer lichens or modification of stress responses in plants.

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Publication

Klaas Yperman *, Jie Wang *, Dominique Eeckhout, Joanna Winkler, Lam Dai Vu, Michael Vandorpe, Peter Grones, Evelien Mylle, Michael Kraus, Romain Merceron, Jonah Nolf, Eliana Mor, Pieter De Bruyn, Remy Loris, Martin Potocký, Savvas N. Savvides, Bert De Rybel, Geert De Jaeger, Daniël Van Damme and Roman Pleskot (2021). Molecular architecture of the endocytic TPLATE complex. Advances in science. DOI: 10.1126 / sciadv.abe7999.

Funding

The study is funded by a grant from T-REX ERC Consolidator (682436) and by the National Science Foundation Flanders (FWO; G009415N). Jie Wang was supported by the China Scholarship Council (grant number 201508440249 to JW) and co-funded by the Ghent University CSC BOF (grant number ST01511051). Peter Grones with FWO grant (3E004619) and Martin Potocký with Czech science foundation grant (GA19-21758S).

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